Chicken Feathers Extraction

CHAPTER I

INTRODUCTION

RESEARCH BACKGROUND

This research is about the extraction of keratin protein from chicken feathers using strong fluid extraction process. This extraction procedure utilized a dissolvable as lessening specialists to separate salt linkages, disulphide bond and hydrogen bond of the keratin fiber to break down into protein. Thus, it will likewise diminish the steadiness of keratin strands in the strong structure found in feathers.

Proteins are polymer formed by one or more long chains of amino acid residues that are capable of promoting intra- and inter-molecular bonds so that it allows the resultant materials to have a large variation in their functional properties. Amino acids linked together by peptide bonds,

The demand of the chicken is increasing throughout the year from the consumer. Poultry factory produce large amount of feather. The uncontrolled disposal used such as land filling and incineration or burial cause many problems in storage, handling, emission control and ash problem that lead to pollution in our environment. According to (reference), Five percent of the body weight of poultry is feather. Discarded feathers will also cause various infections including chlorosis, mycoplasmosis and fowl cholera. Based on the report by (reference), almost 91% of chicken feather consists of keratin, thus it would be an interesting attempt to extract this protein from the chicken feathers. Rather than being disposed of as a waste, valuable product such as protein keratin can be discovered from the chicken

In addition, natural proteins are the most suitable for cosmetic uses than the other two proteins which are conjugated proteins and derived proteins. Figure 2.2: Normal protein sources

Proteins are divided into four categories of structures. Primary structure, secondary structure, tertiary structure and the last one quaternary structure.
Primary structure: the linear arrangement of amino acids presents in a polypeptide chain and the location of covalent linkages such as disulfide bonds between amino acids.
Secondary structure: areas of folding or coiling within a protein with examples include alpha helices and pleated sheets, which are stabilized by hydrogen bonding.
Tertiary structure: the final three-dimensional structure of a protein, which results from a large number of non-covalent interactions between amino acids.
Quaternary structure: non-covalent interactions that bind multiple polypeptides into a single, larger protein. Hemoglobin has quaternary structure due to association of two alpha globin and two beta globin polyproteins.

2.3